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2boo
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2boo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2boo, resolution 1.80Å" /> '''THE CRYSTAL STRUCTU...) |
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| - | [[Image:2boo.gif|left|200px]]<br /> | ||
| - | <applet load="2boo" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2boo, resolution 1.80Å" /> | ||
| - | '''THE CRYSTAL STRUCTURE OF URACIL-DNA N-GLYCOSYLASE (UNG) FROM DEINOCOCCUS RADIODURANS.'''<br /> | ||
| - | == | + | ==The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans.== |
| - | Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal | + | <StructureSection load='2boo' size='340' side='right'caption='[[2boo]], [[Resolution|resolution]] 1.80Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2boo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BOO FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2boo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2boo OCA], [https://pdbe.org/2boo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2boo RCSB], [https://www.ebi.ac.uk/pdbsum/2boo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2boo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/UNG_DEIRA UNG_DEIRA] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/2boo_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2boo ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal of promutagenic uracil from single- and double-stranded DNA, thereby initiating the base-excision repair (BER) pathway. Uracil in DNA can occur by mis-incorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs. The radiation-resistant bacterium Deinococcus radiodurans has an elevated number of uracil-DNA glycosylases compared with most other organisms. The crystal structure of dr0689 (uracil-DNA N-glycosylase), which has been shown to be the major contributor to the removal of mis-incorporated uracil bases in crude cell extracts of D. radiodurans, is reported. | ||
| - | + | Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans.,Leiros I, Moe E, Smalas AO, McSweeney S Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1049-56. Epub 2005, Jul 20. PMID:16041069<ref>PMID:16041069</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2boo" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Deinococcus radiodurans R1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Leiros I]] | ||
| + | [[Category: McSweeney S]] | ||
| + | [[Category: Moe E]] | ||
| + | [[Category: Smalas AO]] | ||
Current revision
The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans.
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